摘要翻译：
我们发现，排除体积效应、疏水性和管状多肽链的氢键之间的相互作用产生了自由能景观，这些景观显示出与蛋白质中常见的结构基序相对应的少量亚稳极小值。景观的复杂性只随链的长度适度增加。对这些景观的温度依赖性的分析表明，在接近折叠中点的温度下，特定亚稳态的稳定性最大。因此，这些可稳定状态可能在确定蛋白质聚集成潜在致病剂的一般性趋势方面具有特别重要的意义。
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英文标题：
《Importance of Metastable States in the Free Energy Landscapes of
  Polypeptide Chains》
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作者：
Stefan Auer, Mark A. Miller, Sergei V. Krivov, Christopher M. Dobson,
  Martin Karplus and Michele Vendruscolo
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最新提交年份：
2007
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分类信息：

一级分类：Physics        物理学
二级分类：Soft Condensed Matter        软凝聚态物质
分类描述：Membranes, polymers, liquid crystals, glasses, colloids, granular matter
膜，聚合物，液晶，玻璃，胶体，颗粒物质
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一级分类：Physics        物理学
二级分类：Statistical Mechanics        统计力学
分类描述：Phase transitions, thermodynamics, field theory, non-equilibrium phenomena, renormalization group and scaling, integrable models, turbulence
相变，热力学，场论，非平衡现象，重整化群和标度，可积模型，湍流
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英文摘要：
  We show that the interplay between excluded volume effects, hydrophobicity, and hydrogen bonding of a tube-like representation of a polypeptide chain gives rise to free energy landscapes that exhibit a small number of metastable minima corresponding to common structural motifs observed in proteins. The complexity of the landscape increases only moderately with the length of the chain. Analysis of the temperature dependence of these landscapes reveals that the stability of specific metastable states is maximal at a temperature close to the mid-point of folding. These mestastable states are therefore likely to be of particular significance in determining the generic tendency of proteins to aggregate into potentially pathogenic agents.
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PDF链接：
https://arxiv.org/pdf/710.3532